A glycoprotein in the plasma membrane matrix as a major potential substrate of p60v-src

Michinari Hamaguchi, Michiyuki Matsuda, Hidesaburo Hanafusa

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    14 Scopus citations


    A potential substrate of p60v-src in Rous sarcoma virus-transformed cells was found to be a 130-kilodalton (kDa) glycoprotein which binds to lectin-Sepharose and can be immunoprecipitated by an anti-phosphotyrosine antibody. This glycoprotein was shown to be distinct from the flbronectin receptor and a cellular protein phosphorylated in p60v-src immune complexes. The protein was a transmembrane protein localized in the plasma membrane and resistant to extraction with Triton X-100. The 130-kDa protein was also highly phosphorylated in cells transformed by Fujinami sarcoma virus or Y73 but not in cells infected with Rous sarcoma virus mutants that encode p60v-src lacking myristoylated N termini. Phosphorylation of this glycoprotein was temperature dependent in cells infected with temperature-sensitive mutants. The good correlation between its phosphorylation and morphological transformation, together with its relative abundance among phosphorylated proteins and its subcellular localization, suggests that phosphorylation of the 130-kDa glycoprotein is one of the primary events important for cell transformation by p60v-src and related oncogene products.

    Original languageEnglish (US)
    Pages (from-to)830-836
    Number of pages7
    JournalMolecular and cellular biology
    Issue number2
    StatePublished - Feb 1990


    ASJC Scopus subject areas

    • Molecular Biology
    • Cell Biology

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